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Interaction of a peptidomimetic aminimide inhibitor with elastase
E Peisach1, D Casebier, S L Gallion
1Program in Biophysics, Brandeis University, Waltham, MA 02254, USA.
Science (New York, N.Y.)
|July 7, 1995
Abstract:
The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design.